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Volumn 15, Issue , 2005, Pages 203-228

Extracellular matrix and the development of disease: The role of its components in cancer progression

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EID: 33750915458     PISSN: 15743349     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1574-3349(05)15007-8     Document Type: Review
Times cited : (3)

References (170)
  • 1
    • 0027491441 scopus 로고
    • Identification of a novel collagen chain represented by extensive interruptions in the triple-helical region
    • Abe N., Muragaki Y., Yoshioka H., Inoue H., and Ninomiya Y. Identification of a novel collagen chain represented by extensive interruptions in the triple-helical region. Biochem. Biophys. Res. Commun. 196 (1993) 576-582
    • (1993) Biochem. Biophys. Res. Commun. , vol.196 , pp. 576-582
    • Abe, N.1    Muragaki, Y.2    Yoshioka, H.3    Inoue, H.4    Ninomiya, Y.5
  • 2
    • 0034118422 scopus 로고    scopus 로고
    • Type XV collagen in human colonic adenocarcinomas has a different distribution than other basement membrane zone proteins
    • Amenta P.S., Briggs K., Xu K., Gamboa E., Jukkola A.F., Li D., and Myers J.C. Type XV collagen in human colonic adenocarcinomas has a different distribution than other basement membrane zone proteins. Hum. Pathol. 31 (2000) 359-366
    • (2000) Hum. Pathol. , vol.31 , pp. 359-366
    • Amenta, P.S.1    Briggs, K.2    Xu, K.3    Gamboa, E.4    Jukkola, A.F.5    Li, D.6    Myers, J.C.7
  • 3
    • 0037371896 scopus 로고    scopus 로고
    • Loss of types XV and XIX collagen precedes basement membrane invasion in ductal carcinoma of the female breast
    • Amenta P.S., Hadad S., Lee M.T., Barnard N., Li D., and Myers J.C. Loss of types XV and XIX collagen precedes basement membrane invasion in ductal carcinoma of the female breast. J. Pathol. 199 (2003) 298-308
    • (2003) J. Pathol. , vol.199 , pp. 298-308
    • Amenta, P.S.1    Hadad, S.2    Lee, M.T.3    Barnard, N.4    Li, D.5    Myers, J.C.6
  • 4
    • 0037361399 scopus 로고    scopus 로고
    • Laminin 5 processing and its integration into the ECM
    • Aumailley M., El Khal A., Knoss N., and Tunggal L. Laminin 5 processing and its integration into the ECM. Matrix Biol. 22 (2003) 49-54
    • (2003) Matrix Biol. , vol.22 , pp. 49-54
    • Aumailley, M.1    El Khal, A.2    Knoss, N.3    Tunggal, L.4
  • 5
    • 0032401813 scopus 로고    scopus 로고
    • Association of the decreased expression of alpha3beta1 integrin with the altered cell: Environmental interactions and enhanced soft agar cloning ability of c-myc-overexpressing small cell lung cancer cells
    • Barr L.F., Campbell S.E., Bochner B.S., and Dang C.V. Association of the decreased expression of alpha3beta1 integrin with the altered cell: Environmental interactions and enhanced soft agar cloning ability of c-myc-overexpressing small cell lung cancer cells. Cancer Res. 58 (1998) 5537-5545
    • (1998) Cancer Res. , vol.58 , pp. 5537-5545
    • Barr, L.F.1    Campbell, S.E.2    Bochner, B.S.3    Dang, C.V.4
  • 6
    • 0025165018 scopus 로고
    • Structure and function of laminin: Anatomy of a multidomain glycoprotein
    • Beck K., Hunter I., and Engel J. Structure and function of laminin: Anatomy of a multidomain glycoprotein. FASEB J. 4 (1990) 148-160
    • (1990) FASEB J. , vol.4 , pp. 148-160
    • Beck, K.1    Hunter, I.2    Engel, J.3
  • 7
    • 1842787815 scopus 로고    scopus 로고
    • The urokinase receptor (uPAR) and the uPAR-associated protein (uPARAP/Endo180): Membrane proteins engaged in matrix turnover during tissue remodeling
    • Behrendt N. The urokinase receptor (uPAR) and the uPAR-associated protein (uPARAP/Endo180): Membrane proteins engaged in matrix turnover during tissue remodeling. Biol. Chem. 385 (2004) 103-136
    • (2004) Biol. Chem. , vol.385 , pp. 103-136
    • Behrendt, N.1
  • 8
    • 0030344838 scopus 로고    scopus 로고
    • Cathepsin B expression in human tumors
    • Berquin I.M., and Sloane B.F. Cathepsin B expression in human tumors. Adv. Exp. Med. Biol. 389 (1996) 281-294
    • (1996) Adv. Exp. Med. Biol. , vol.389 , pp. 281-294
    • Berquin, I.M.1    Sloane, B.F.2
  • 9
    • 0036990109 scopus 로고    scopus 로고
    • The organizing principle: Microenvironmental influences in the normal and malignant breast
    • Bissell M.J., Radisky D.C., Rizki A., Weaver V.M., and Petersen O.W. The organizing principle: Microenvironmental influences in the normal and malignant breast. Differentiation 70 (2002) 537-546
    • (2002) Differentiation , vol.70 , pp. 537-546
    • Bissell, M.J.1    Radisky, D.C.2    Rizki, A.3    Weaver, V.M.4    Petersen, O.W.5
  • 10
    • 0035958849 scopus 로고    scopus 로고
    • The NC1 domain of collagen IV encodes a novel network composed of the alpha 1, alpha 2, alpha 5, and alpha 6 chains in smooth muscle basement membranes
    • Borza D.B., Bondar O., Ninomiya Y., Sado Y., Naito I., Todd P., and Hudson B.G. The NC1 domain of collagen IV encodes a novel network composed of the alpha 1, alpha 2, alpha 5, and alpha 6 chains in smooth muscle basement membranes. J. Biol. Chem. 276 (2001) 28532-28540
    • (2001) J. Biol. Chem. , vol.276 , pp. 28532-28540
    • Borza, D.B.1    Bondar, O.2    Ninomiya, Y.3    Sado, Y.4    Naito, I.5    Todd, P.6    Hudson, B.G.7
  • 11
    • 0037131174 scopus 로고    scopus 로고
    • Quaternary organization of the goodpasture autoantigen, the alpha 3(IV) collagen chain. Sequestration of two cryptic autoepitopes by intrapromoter interactions with the alpha4 and alpha5 NC1 domains
    • Borza D.B., Bondar O., Todd P., Sundaramoorthy M., Sado Y., Ninomiya Y., and Hudson B.G. Quaternary organization of the goodpasture autoantigen, the alpha 3(IV) collagen chain. Sequestration of two cryptic autoepitopes by intrapromoter interactions with the alpha4 and alpha5 NC1 domains. J. Biol. Chem. 277 (2002) 40075-40083
    • (2002) J. Biol. Chem. , vol.277 , pp. 40075-40083
    • Borza, D.B.1    Bondar, O.2    Todd, P.3    Sundaramoorthy, M.4    Sado, Y.5    Ninomiya, Y.6    Hudson, B.G.7
  • 12
    • 0038575444 scopus 로고    scopus 로고
    • Functional structure and composition of the extracellular matrix
    • Bosman F.T., and Stamenkovic I. Functional structure and composition of the extracellular matrix. J. Pathol. 200 (2003) 423-428
    • (2003) J. Pathol. , vol.200 , pp. 423-428
    • Bosman, F.T.1    Stamenkovic, I.2
  • 13
    • 0034730769 scopus 로고    scopus 로고
    • Type IV collagen of the glomerular basement membrane. Evidence that the chain specificity of network assembly is encoded by the noncollagenous NC1 domains
    • Boutaud A., Borza D.B., Bondar O., Gunwar S., Netzer K.O., Singh N., Ninomiya Y., Sado Y., Noelken M.E., and Hudson B.G. Type IV collagen of the glomerular basement membrane. Evidence that the chain specificity of network assembly is encoded by the noncollagenous NC1 domains. J. Biol. Chem. 275 (2000) 30716-30724
    • (2000) J. Biol. Chem. , vol.275 , pp. 30716-30724
    • Boutaud, A.1    Borza, D.B.2    Bondar, O.3    Gunwar, S.4    Netzer, K.O.5    Singh, N.6    Ninomiya, Y.7    Sado, Y.8    Noelken, M.E.9    Hudson, B.G.10
  • 14
    • 0028670833 scopus 로고
    • Integrin alpha v beta 3 antagonists promote tumor regression by inducing apoptosis of angiogenic blood vessels
    • Brooks P.C., Montgomery A.M., Rosenfeld M., Reisfeld R.A., Hu T., Klier G., and Cheresh D.A. Integrin alpha v beta 3 antagonists promote tumor regression by inducing apoptosis of angiogenic blood vessels. Cell 79 (1994) 1157-1164
    • (1994) Cell , vol.79 , pp. 1157-1164
    • Brooks, P.C.1    Montgomery, A.M.2    Rosenfeld, M.3    Reisfeld, R.A.4    Hu, T.5    Klier, G.6    Cheresh, D.A.7
  • 15
    • 0010712792 scopus 로고    scopus 로고
    • Disruption of angiogenesis by PEX, a noncatalytic metalloproteinase fragment with integrin binding activity
    • Brooks P.C., Silletti S., von Schalscha T.L., Friedlander M., and Cheresh D.A. Disruption of angiogenesis by PEX, a noncatalytic metalloproteinase fragment with integrin binding activity. Cell 92 (1998) 391-400
    • (1998) Cell , vol.92 , pp. 391-400
    • Brooks, P.C.1    Silletti, S.2    von Schalscha, T.L.3    Friedlander, M.4    Cheresh, D.A.5
  • 16
    • 0042411037 scopus 로고    scopus 로고
    • Laminin, hyaluronan, tenascin-C and type VI collagen levels in sera from patients with malignant melanoma
    • Burchardt E.R., Hein R., and Bosserhoff A.K. Laminin, hyaluronan, tenascin-C and type VI collagen levels in sera from patients with malignant melanoma. Clin. Exp. Dermatol. 28 (2003) 515-520
    • (2003) Clin. Exp. Dermatol. , vol.28 , pp. 515-520
    • Burchardt, E.R.1    Hein, R.2    Bosserhoff, A.K.3
  • 17
    • 0025294641 scopus 로고
    • Characterization of a synthetic peptide from type IV collagen that promotes melanoma cell adhesion, spreading, and motility
    • Chelberg M.K., McCarthy J.B., Skubitz A.P., Furcht L.T., and Tsilibary E.C. Characterization of a synthetic peptide from type IV collagen that promotes melanoma cell adhesion, spreading, and motility. J. Cell. Biol. 111 (1990) 261-270
    • (1990) J. Cell. Biol. , vol.111 , pp. 261-270
    • Chelberg, M.K.1    McCarthy, J.B.2    Skubitz, A.P.3    Furcht, L.T.4    Tsilibary, E.C.5
  • 18
    • 0024365672 scopus 로고
    • Type IV collagen-mediated melanoma cell adhesion and migration: Involvement of multiple, distinct domains of the collagen molecule
    • Chelberg M.K., Tsilibary E.C., Hauser A.R., and McCarthy J.B. Type IV collagen-mediated melanoma cell adhesion and migration: Involvement of multiple, distinct domains of the collagen molecule. Cancer Res. 49 (1989) 4796-4802
    • (1989) Cancer Res. , vol.49 , pp. 4796-4802
    • Chelberg, M.K.1    Tsilibary, E.C.2    Hauser, A.R.3    McCarthy, J.B.4
  • 19
    • 0142188116 scopus 로고    scopus 로고
    • Urokinase plasminogen activator system: a multifunctional role in tumor progression and metastasis
    • Choong P.F., and Nadesapillai A.P. Urokinase plasminogen activator system: a multifunctional role in tumor progression and metastasis. Clin. Orthop. (2003) S46-S58
    • (2003) Clin. Orthop.
    • Choong, P.F.1    Nadesapillai, A.P.2
  • 22
    • 0029968743 scopus 로고    scopus 로고
    • Combined overexpression of urokinase, urokinase receptor, and plasminogen activator inhibitor-1 is associated with breast cancer progression: An immunohistochemical comparison of normal, benign, and malignant breast tissues
    • Costantini V., Sidoni A., Deveglia R., Cazzato O.A., Bellezza G., Ferri I., Bucciarelli E., and Nenci G.G. Combined overexpression of urokinase, urokinase receptor, and plasminogen activator inhibitor-1 is associated with breast cancer progression: An immunohistochemical comparison of normal, benign, and malignant breast tissues. Cancer 77 (1996) 1079-1088
    • (1996) Cancer , vol.77 , pp. 1079-1088
    • Costantini, V.1    Sidoni, A.2    Deveglia, R.3    Cazzato, O.A.4    Bellezza, G.5    Ferri, I.6    Bucciarelli, E.7    Nenci, G.G.8
  • 23
    • 0037192458 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors and cancer: Trials and tribulations
    • Coussens L.M., Fingleton B., and Matrisian L.M. Matrix metalloproteinase inhibitors and cancer: Trials and tribulations. Science 295 (2002) 2387-2392
    • (2002) Science , vol.295 , pp. 2387-2392
    • Coussens, L.M.1    Fingleton, B.2    Matrisian, L.M.3
  • 24
    • 0037899253 scopus 로고    scopus 로고
    • Role of tissue stroma in cancer cell invasion
    • De Wever O., and Mareel M. Role of tissue stroma in cancer cell invasion. J. Pathol. 200 (2003) 429-447
    • (2003) J. Pathol. , vol.200 , pp. 429-447
    • De Wever, O.1    Mareel, M.2
  • 26
    • 0034255167 scopus 로고    scopus 로고
    • Immunostained cathepsins B and L correlate with depth of invasion and different metastatic pathways in early stage gastric carcinoma
    • Dohchin A., Suzuki J.I., Seki H., Masutani M., Shiroto H., and Kawakami Y. Immunostained cathepsins B and L correlate with depth of invasion and different metastatic pathways in early stage gastric carcinoma. Cancer 89 (2000) 482-487
    • (2000) Cancer , vol.89 , pp. 482-487
    • Dohchin, A.1    Suzuki, J.I.2    Seki, H.3    Masutani, M.4    Shiroto, H.5    Kawakami, Y.6
  • 27
    • 0030998660 scopus 로고    scopus 로고
    • Macrophage-derived metalloelastase is responsible for the generation of angiostatin in Lewis lung carcinoma
    • Dong Z., Kumar R., Yang X., and Fidler I.J. Macrophage-derived metalloelastase is responsible for the generation of angiostatin in Lewis lung carcinoma. Cell 88 (1997) 801-810
    • (1997) Cell , vol.88 , pp. 801-810
    • Dong, Z.1    Kumar, R.2    Yang, X.3    Fidler, I.J.4
  • 28
    • 2942751908 scopus 로고    scopus 로고
    • Pro-MMP-9 is a specific macrophage product and is activated by osteoarthritic chondrocytes via MMP-3 or a MT1-MMP/MMP-13 cascade
    • Dreier R., Grassel S., Fuchs S., Schaumburger J., and Bruckner P. Pro-MMP-9 is a specific macrophage product and is activated by osteoarthritic chondrocytes via MMP-3 or a MT1-MMP/MMP-13 cascade. Exp. Cell. Res. 297 (2004) 303-312
    • (2004) Exp. Cell. Res. , vol.297 , pp. 303-312
    • Dreier, R.1    Grassel, S.2    Fuchs, S.3    Schaumburger, J.4    Bruckner, P.5
  • 29
    • 0027378858 scopus 로고
    • The alpha 1 beta 1 integrin recognition site of the basement membrane collagen molecule [alpha 1(IV)]2 alpha 2(IV)
    • Eble J.A., Golbik R., Mann K., and Kuhn K. The alpha 1 beta 1 integrin recognition site of the basement membrane collagen molecule [alpha 1(IV)]2 alpha 2(IV). EMBO J. 12 (1993) 4795-4802
    • (1993) EMBO J. , vol.12 , pp. 4795-4802
    • Eble, J.A.1    Golbik, R.2    Mann, K.3    Kuhn, K.4
  • 30
    • 0037096888 scopus 로고    scopus 로고
    • The B16F10 cell receptor for a metastasis-promoting site on laminin-1 is a heparan sulfate/chondroitin sulfate-containing proteoglycan
    • Engbring J.A., Hoffman M.P., Karmand A.J., and Kleinman H.K. The B16F10 cell receptor for a metastasis-promoting site on laminin-1 is a heparan sulfate/chondroitin sulfate-containing proteoglycan. Cancer Res. 62 (2002) 3549-3554
    • (2002) Cancer Res. , vol.62 , pp. 3549-3554
    • Engbring, J.A.1    Hoffman, M.P.2    Karmand, A.J.3    Kleinman, H.K.4
  • 31
    • 0038236716 scopus 로고    scopus 로고
    • The basement membrane matrix in malignancy
    • Engbring J.A., and Kleinman H.K. The basement membrane matrix in malignancy. J. Pathol. 200 (2003) 465-470
    • (2003) J. Pathol. , vol.200 , pp. 465-470
    • Engbring, J.A.1    Kleinman, H.K.2
  • 32
    • 0037432127 scopus 로고    scopus 로고
    • Angiostatin and endostatin inhibit endothelial cell migration in response to FGF and VEGF without interfering with specific intracellular signal transduction pathways
    • Eriksson K., Magnusson P., Dixelius J., Claesson-Welsh L., and Cross M.J. Angiostatin and endostatin inhibit endothelial cell migration in response to FGF and VEGF without interfering with specific intracellular signal transduction pathways. FEBS Lett. 536 (2003) 19-24
    • (2003) FEBS Lett. , vol.536 , pp. 19-24
    • Eriksson, K.1    Magnusson, P.2    Dixelius, J.3    Claesson-Welsh, L.4    Cross, M.J.5
  • 33
    • 0034013621 scopus 로고    scopus 로고
    • A peptide of the alpha 3(IV) chain of type IV collagen modulates stimulated neutrophil function via activation of cAMP-dependent protein kinase and Ser/Thr protein phosphatase
    • Fawzi A., Robinet A., Monboisse J.C., Ziaie Z., Kefalides N.A., and Bellon G. A peptide of the alpha 3(IV) chain of type IV collagen modulates stimulated neutrophil function via activation of cAMP-dependent protein kinase and Ser/Thr protein phosphatase. Cell Signal 12 (2000) 327-335
    • (2000) Cell Signal , vol.12 , pp. 327-335
    • Fawzi, A.1    Robinet, A.2    Monboisse, J.C.3    Ziaie, Z.4    Kefalides, N.A.5    Bellon, G.6
  • 35
    • 0037278885 scopus 로고    scopus 로고
    • Integrin adhesion receptors in tumor metastasis
    • Felding-Habermann B. Integrin adhesion receptors in tumor metastasis. Clin. Exp. Metastasis 20 (2003) 203-213
    • (2003) Clin. Exp. Metastasis , vol.20 , pp. 203-213
    • Felding-Habermann, B.1
  • 37
    • 0034672644 scopus 로고    scopus 로고
    • Generation and degradation of human endostatin proteins by various proteinases
    • Ferreras M., Felbor U., Lenhard T., Olsen B.R., and Delaisse J. Generation and degradation of human endostatin proteins by various proteinases. FEBS Lett. 486 (2000) 247-251
    • (2000) FEBS Lett. , vol.486 , pp. 247-251
    • Ferreras, M.1    Felbor, U.2    Lenhard, T.3    Olsen, B.R.4    Delaisse, J.5
  • 38
  • 39
    • 5444219883 scopus 로고    scopus 로고
    • Matrix metalloproteinases in cancer: From new functions to improved inhibition strategies
    • Folgueras A.R., Pendas A.M., Sanchez L.M., and Lopez-Otin C. Matrix metalloproteinases in cancer: From new functions to improved inhibition strategies. Int. J. Dev. Biol. 48 (2004) 411-424
    • (2004) Int. J. Dev. Biol. , vol.48 , pp. 411-424
    • Folgueras, A.R.1    Pendas, A.M.2    Sanchez, L.M.3    Lopez-Otin, C.4
  • 42
    • 0026542056 scopus 로고
    • Integrin expression in human melanoma cells with differing invasive and metastatic properties
    • Gehlsen K.R., Davis G.E., and Sriramarao P. Integrin expression in human melanoma cells with differing invasive and metastatic properties. Clin. Exp. Metastasis 10 (1992) 111-120
    • (1992) Clin. Exp. Metastasis , vol.10 , pp. 111-120
    • Gehlsen, K.R.1    Davis, G.E.2    Sriramarao, P.3
  • 43
    • 0034333019 scopus 로고    scopus 로고
    • Proteolytic modification of laminins: Functional consequences
    • Ghosh S., and Stack M.S. Proteolytic modification of laminins: Functional consequences. Microsc. Res. Tech. 51 (2000) 238-246
    • (2000) Microsc. Res. Tech. , vol.51 , pp. 238-246
    • Ghosh, S.1    Stack, M.S.2
  • 45
    • 0032900372 scopus 로고    scopus 로고
    • Expression of matrix metalloprotease-2-cleaved laminin-5 in breast remodeling stimulated by sex steroids
    • Giannelli G., Pozzi A., Stetler-Stevenson W.G., Gardner H.A., and Quaranta V. Expression of matrix metalloprotease-2-cleaved laminin-5 in breast remodeling stimulated by sex steroids. Am. J. Pathol. 154 (1999) 1193-1201
    • (1999) Am. J. Pathol. , vol.154 , pp. 1193-1201
    • Giannelli, G.1    Pozzi, A.2    Stetler-Stevenson, W.G.3    Gardner, H.A.4    Quaranta, V.5
  • 47
    • 0032489876 scopus 로고    scopus 로고
    • Processing of laminin-5 and its functional consequences: Role of plasmin and tissue-type plasminogen activator
    • Goldfinger L.E., Stack M.S., and Jones J.C. Processing of laminin-5 and its functional consequences: Role of plasmin and tissue-type plasminogen activator. J. Cell. Biol. 141 (1998) 255-265
    • (1998) J. Cell. Biol. , vol.141 , pp. 255-265
    • Goldfinger, L.E.1    Stack, M.S.2    Jones, J.C.3
  • 49
    • 0032566501 scopus 로고    scopus 로고
    • Collagen XVIII is a basement membrane heparan sulfate proteoglycan
    • Halfter W., Dong S., Schurer B., and Cole G.J. Collagen XVIII is a basement membrane heparan sulfate proteoglycan. J. Biol. Chem. 273 (1998) 25404-25412
    • (1998) J. Biol. Chem. , vol.273 , pp. 25404-25412
    • Halfter, W.1    Dong, S.2    Schurer, B.3    Cole, G.J.4
  • 50
    • 10744223801 scopus 로고    scopus 로고
    • Physiological levels of tumstatin, a fragment of collagen IV alpha3 chain, are generated by MMP-9 proteolysis and suppress angiogenesis via alphaV beta3 integrin
    • Hamano Y., Zeisberg M., Sugimoto H., Lively J.C., Maeshima Y., Yang C., Hynes R.O., Werb Z., Sudhakar A., and Kalluri R. Physiological levels of tumstatin, a fragment of collagen IV alpha3 chain, are generated by MMP-9 proteolysis and suppress angiogenesis via alphaV beta3 integrin. Cancer Cell 3 (2003) 589-601
    • (2003) Cancer Cell , vol.3 , pp. 589-601
    • Hamano, Y.1    Zeisberg, M.2    Sugimoto, H.3    Lively, J.C.4    Maeshima, Y.5    Yang, C.6    Hynes, R.O.7    Werb, Z.8    Sudhakar, A.9    Kalluri, R.10
  • 51
    • 0030753192 scopus 로고    scopus 로고
    • A cell binding domain from the alpha3 chain of type IV collagen inhibits proliferation of melanoma cells
    • Han J., Ohno N., Pasco S., Monboisse J.C., Borel J.P., and Kefalides N.A. A cell binding domain from the alpha3 chain of type IV collagen inhibits proliferation of melanoma cells. J. Biol. Chem. 272 (1997) 20395-20401
    • (1997) J. Biol. Chem. , vol.272 , pp. 20395-20401
    • Han, J.1    Ohno, N.2    Pasco, S.3    Monboisse, J.C.4    Borel, J.P.5    Kefalides, N.A.6
  • 52
    • 0035103373 scopus 로고    scopus 로고
    • Investigation into the mechanism of the loss of laminin 5 (alpha3beta3gamma2) expression in prostate cancer
    • Hao J., Jackson L., Calaluce R., McDaniel K., Dalkin B.L., and Nagle R.B. Investigation into the mechanism of the loss of laminin 5 (alpha3beta3gamma2) expression in prostate cancer. Am. J. Pathol. 158 (2001) 1129-1135
    • (2001) Am. J. Pathol. , vol.158 , pp. 1129-1135
    • Hao, J.1    Jackson, L.2    Calaluce, R.3    McDaniel, K.4    Dalkin, B.L.5    Nagle, R.B.6
  • 53
    • 0029833668 scopus 로고    scopus 로고
    • Differential expression of laminin 5 (alpha 3 beta 3 gamma 2) by human malignant and normal prostate
    • Hao J., Yang Y., McDaniel K.M., Dalkin B.L., Cress A.E., and Nagle R.B. Differential expression of laminin 5 (alpha 3 beta 3 gamma 2) by human malignant and normal prostate. Am. J. Pathol. 149 (1996) 1341-1349
    • (1996) Am. J. Pathol. , vol.149 , pp. 1341-1349
    • Hao, J.1    Yang, Y.2    McDaniel, K.M.3    Dalkin, B.L.4    Cress, A.E.5    Nagle, R.B.6
  • 54
    • 2142757236 scopus 로고    scopus 로고
    • The C-terminal domain of canstatin suppresses in vivo tumor growth associated with proliferation of endothelial cells
    • He G.A., Luo J.X., Zhang T.Y., Hu Z.S., and Wang F.Y. The C-terminal domain of canstatin suppresses in vivo tumor growth associated with proliferation of endothelial cells. Biochem. Biophys. Res. Commun. 318 (2004) 354-360
    • (2004) Biochem. Biophys. Res. Commun. , vol.318 , pp. 354-360
    • He, G.A.1    Luo, J.X.2    Zhang, T.Y.3    Hu, Z.S.4    Wang, F.Y.5
  • 55
    • 0344983831 scopus 로고    scopus 로고
    • Canstatin-N fragment inhibits in vitro endothelial cell proliferation and suppresses in vivo tumor growth
    • He G.A., Luo J.X., Zhang T.Y., Wang F.Y., and Li R.F. Canstatin-N fragment inhibits in vitro endothelial cell proliferation and suppresses in vivo tumor growth. Biochem. Biophys. Res. Commun. 312 (2003) 801-805
    • (2003) Biochem. Biophys. Res. Commun. , vol.312 , pp. 801-805
    • He, G.A.1    Luo, J.X.2    Zhang, T.Y.3    Wang, F.Y.4    Li, R.F.5
  • 56
    • 3142742372 scopus 로고    scopus 로고
    • Identification of an active site on the laminin alpha5 chain globular domain that binds to CD44 and inhibits malignancy
    • Hibino S., Shibuya M., Engbring J.A., Mochizuki M., Nomizu M., and Kleinman H.K. Identification of an active site on the laminin alpha5 chain globular domain that binds to CD44 and inhibits malignancy. Cancer Res. 64 (2004) 4810-4816
    • (2004) Cancer Res. , vol.64 , pp. 4810-4816
    • Hibino, S.1    Shibuya, M.2    Engbring, J.A.3    Mochizuki, M.4    Nomizu, M.5    Kleinman, H.K.6
  • 57
    • 0036962220 scopus 로고    scopus 로고
    • Differential distribution of basement membrane type IV collagen alpha1(IV), alpha2(IV), alpha5(IV) and alpha6(IV) chains in colorectal epithelial tumors
    • Hiki Y., Iyama K., Tsuruta J., Egami H., Kamio T., Suko S., Naito I., Sado Y., Ninomiya Y., and Ogawa M. Differential distribution of basement membrane type IV collagen alpha1(IV), alpha2(IV), alpha5(IV) and alpha6(IV) chains in colorectal epithelial tumors. Pathol. Int. 52 (2002) 224-233
    • (2002) Pathol. Int. , vol.52 , pp. 224-233
    • Hiki, Y.1    Iyama, K.2    Tsuruta, J.3    Egami, H.4    Kamio, T.5    Suko, S.6    Naito, I.7    Sado, Y.8    Ninomiya, Y.9    Ogawa, M.10
  • 58
    • 3042749811 scopus 로고    scopus 로고
    • Epithelial cell motility on laminin-5: regulation by matrix assembly, proteolysis, integrins and erbB receptors
    • Hintermann E., and Quaranta V. Epithelial cell motility on laminin-5: regulation by matrix assembly, proteolysis, integrins and erbB receptors. Matrix Biol. 23 (2004) 75-85
    • (2004) Matrix Biol. , vol.23 , pp. 75-85
    • Hintermann, E.1    Quaranta, V.2
  • 59
    • 0036166823 scopus 로고    scopus 로고
    • Domain structure and organisation in extracellular matrix proteins
    • Hohenester E., and Engel J. Domain structure and organisation in extracellular matrix proteins. Matrix Biol. 21 (2002) 115-128
    • (2002) Matrix Biol. , vol.21 , pp. 115-128
    • Hohenester, E.1    Engel, J.2
  • 60
    • 0036488589 scopus 로고    scopus 로고
    • Role of integrins in cell invasion and migration
    • Hood J.D., and Cheresh D.A. Role of integrins in cell invasion and migration. Nat. Rev. Cancer 2 (2002) 91-100
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 91-100
    • Hood, J.D.1    Cheresh, D.A.2
  • 61
    • 0024232659 scopus 로고
    • The complete primary structure of the alpha 2 chain of human type IV collagen and comparison with the alpha 1(IV) chain
    • Hostikka S.L., and Tryggvason K. The complete primary structure of the alpha 2 chain of human type IV collagen and comparison with the alpha 1(IV) chain. J. Biol. Chem. 263 (1988) 19488-19493
    • (1988) J. Biol. Chem. , vol.263 , pp. 19488-19493
    • Hostikka, S.L.1    Tryggvason, K.2
  • 62
    • 0036993573 scopus 로고    scopus 로고
    • Melanoma development and progression: a conspiracy between tumor and host
    • Hsu M.Y., Meier F., and Herlyn M. Melanoma development and progression: a conspiracy between tumor and host. Differentiation 70 (2002) 522-536
    • (2002) Differentiation , vol.70 , pp. 522-536
    • Hsu, M.Y.1    Meier, F.2    Herlyn, M.3
  • 63
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: bidirectional, allosteric signaling machines
    • Hynes R. Integrins: bidirectional, allosteric signaling machines. Cell 110 (2002) 673-687
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.1
  • 64
    • 0141866772 scopus 로고    scopus 로고
    • Distinct roles of catalytic and pexin-like domains in membrane-type matrix metalloproteinase (MMP)-mediated pro-MMP-2 activation and collagenolysis
    • Jiang A., and Pei D. Distinct roles of catalytic and pexin-like domains in membrane-type matrix metalloproteinase (MMP)-mediated pro-MMP-2 activation and collagenolysis. J. Biol. Chem. 278 (2003) 38765-38771
    • (2003) J. Biol. Chem. , vol.278 , pp. 38765-38771
    • Jiang, A.1    Pei, D.2
  • 65
    • 1542269303 scopus 로고    scopus 로고
    • Integrins: Roles in cancer development and as treatment targets
    • Jin H., and Varner J. Integrins: Roles in cancer development and as treatment targets. Br. J. Cancer 90 (2004) 561-565
    • (2004) Br. J. Cancer , vol.90 , pp. 561-565
    • Jin, H.1    Varner, J.2
  • 66
    • 0020463650 scopus 로고
    • Extracellular matrix destruction by invasive tumor cells
    • Jones P.A., and De Clerck Y.A. Extracellular matrix destruction by invasive tumor cells. Cancer Metastasis Rev. 1 (1982) 289-317
    • (1982) Cancer Metastasis Rev. , vol.1 , pp. 289-317
    • Jones, P.A.1    De Clerck, Y.A.2
  • 67
    • 0035081580 scopus 로고    scopus 로고
    • Sole expression of laminin gamma 2 chain in invading tumor cells and its association with stromal fibrosis in lung adenocarcinomas
    • Kagesato Y., Mizushima H., Koshikawa N., Kitamura H., Hayashi H., Ogawa N., Tsukuda M., and Miyazaki K. Sole expression of laminin gamma 2 chain in invading tumor cells and its association with stromal fibrosis in lung adenocarcinomas. Jpn. J. Cancer Res. 92 (2001) 184-192
    • (2001) Jpn. J. Cancer Res. , vol.92 , pp. 184-192
    • Kagesato, Y.1    Mizushima, H.2    Koshikawa, N.3    Kitamura, H.4    Hayashi, H.5    Ogawa, N.6    Tsukuda, M.7    Miyazaki, K.8
  • 69
    • 16544391155 scopus 로고    scopus 로고
    • Laminin-5 in epithelial tumour invasion
    • Katayama M., and Sekiguchi K. Laminin-5 in epithelial tumour invasion. J. Mol. Histol. 35 (2004) 277-286
    • (2004) J. Mol. Histol. , vol.35 , pp. 277-286
    • Katayama, M.1    Sekiguchi, K.2
  • 70
    • 0032511257 scopus 로고    scopus 로고
    • Laminin-alpha1-chain sequence Leu-Gln-Val-Gln-Leu-Ser-Ile-Arg (LQVQLSIR) enhances murine melanoma cell metastases
    • Kim W.H., Nomizu M., Song S.Y., Tanaka K., Kuratomi Y., Kleinman H.K., and Yamada Y. Laminin-alpha1-chain sequence Leu-Gln-Val-Gln-Leu-Ser-Ile-Arg (LQVQLSIR) enhances murine melanoma cell metastases. Int. J. Cancer 77 (1998) 632-639
    • (1998) Int. J. Cancer , vol.77 , pp. 632-639
    • Kim, W.H.1    Nomizu, M.2    Song, S.Y.3    Tanaka, K.4    Kuratomi, Y.5    Kleinman, H.K.6    Yamada, Y.7
  • 71
    • 0034307327 scopus 로고    scopus 로고
    • Endostatin inhibits endothelial and tumor cellular invasion by blocking the activation and catalytic activity of matrix metalloproteinase
    • Kim Y.M., Jang J.W., Lee O.H., Yeon J., Choi E.Y., Kim K.W., Lee S.T., and Kwon Y.G. Endostatin inhibits endothelial and tumor cellular invasion by blocking the activation and catalytic activity of matrix metalloproteinase. Cancer Res. 60 (2000) 5410-5413
    • (2000) Cancer Res. , vol.60 , pp. 5410-5413
    • Kim, Y.M.1    Jang, J.W.2    Lee, O.H.3    Yeon, J.4    Choi, E.Y.5    Kim, K.W.6    Lee, S.T.7    Kwon, Y.G.8
  • 72
    • 0028828551 scopus 로고
    • Distribution of type XV collagen transcripts in human tissue and their production by muscle cells and fibroblasts
    • Kivirikko S., Saarela J., Myers J.C., Autio-Harmainen H., and Pihlajaniemi T. Distribution of type XV collagen transcripts in human tissue and their production by muscle cells and fibroblasts. Am. J. Pathol. 147 (1995) 1500-1509
    • (1995) Am. J. Pathol. , vol.147 , pp. 1500-1509
    • Kivirikko, S.1    Saarela, J.2    Myers, J.C.3    Autio-Harmainen, H.4    Pihlajaniemi, T.5
  • 73
    • 0031685364 scopus 로고    scopus 로고
    • Cysteine proteinases and their endogenous inhibitors: Target proteins for prognosis, diagnosis and therapy in cancer (review)
    • Kos J., and Lah T.T. Cysteine proteinases and their endogenous inhibitors: Target proteins for prognosis, diagnosis and therapy in cancer (review). Oncol. Rep. 5 (1998) 1349-13461
    • (1998) Oncol. Rep. , vol.5 , pp. 1349-13461
    • Kos, J.1    Lah, T.T.2
  • 74
    • 0034614939 scopus 로고    scopus 로고
    • Role of cell surface metalloprotease MT1-MMP in epithelial cell migration over laminin-5
    • Koshikawa N., Giannelli G., Cirulli V., Miyazaki K., and Quaranta V. Role of cell surface metalloprotease MT1-MMP in epithelial cell migration over laminin-5. J. Cell. Biol. 148 (2000) 615-624
    • (2000) J. Cell. Biol. , vol.148 , pp. 615-624
    • Koshikawa, N.1    Giannelli, G.2    Cirulli, V.3    Miyazaki, K.4    Quaranta, V.5
  • 75
    • 1442290120 scopus 로고    scopus 로고
    • Proteolytic processing of laminin-5 by MT1-MMP in tissues and its effects on epithelial cell morphology
    • Koshikawa N., Schenk S., Moeckel G., Sharabi A., Miyazaki K., Gardner H., Zent R., and Quaranta V. Proteolytic processing of laminin-5 by MT1-MMP in tissues and its effects on epithelial cell morphology. FASEB J. 18 (2004) 364-366
    • (2004) FASEB J. , vol.18 , pp. 364-366
    • Koshikawa, N.1    Schenk, S.2    Moeckel, G.3    Sharabi, A.4    Miyazaki, K.5    Gardner, H.6    Zent, R.7    Quaranta, V.8
  • 76
    • 0035206434 scopus 로고    scopus 로고
    • Cysteine proteinases in tumor cell growth and apoptosis
    • Krepela E. Cysteine proteinases in tumor cell growth and apoptosis. Neoplasma 48 (2001) 332-349
    • (2001) Neoplasma , vol.48 , pp. 332-349
    • Krepela, E.1
  • 78
    • 0036375021 scopus 로고    scopus 로고
    • Implication of direct host-tumor intercellular interactions in non-immune host resistance to neoplastic growth
    • Krutovskikh V. Implication of direct host-tumor intercellular interactions in non-immune host resistance to neoplastic growth. Semin. Cancer Biol. 12 (2002) 267-276
    • (2002) Semin. Cancer Biol. , vol.12 , pp. 267-276
    • Krutovskikh, V.1
  • 80
    • 85047699539 scopus 로고    scopus 로고
    • Laminin gamma 1 chain peptide, C-16 (KAFDITYVRLKF), promotes migration, MMP-9 secretion, and pulmonary metastasis of B16-F10 mouse melanoma cells
    • Kuratomi Y., Nomizu M., Tanaka K., Ponce M.L., Komiyama S., Kleinman H.K., and Yamada Y. Laminin gamma 1 chain peptide, C-16 (KAFDITYVRLKF), promotes migration, MMP-9 secretion, and pulmonary metastasis of B16-F10 mouse melanoma cells. Br. J. Cancer 86 (2002) 1169-1173
    • (2002) Br. J. Cancer , vol.86 , pp. 1169-1173
    • Kuratomi, Y.1    Nomizu, M.2    Tanaka, K.3    Ponce, M.L.4    Komiyama, S.5    Kleinman, H.K.6    Yamada, Y.7
  • 81
    • 0037515651 scopus 로고    scopus 로고
    • Melanoma cell CD44 interaction with the alpha 1(IV)1263-1277 region from basement membrane collagen is modulated by ligand glycosylation
    • Lauer-Fields J.L., Malkar N.B., Richet G., Drauz K., and Fields G.B. Melanoma cell CD44 interaction with the alpha 1(IV)1263-1277 region from basement membrane collagen is modulated by ligand glycosylation. J. Biol. Chem. 278 (2003) 14321-14330
    • (2003) J. Biol. Chem. , vol.278 , pp. 14321-14330
    • Lauer-Fields, J.L.1    Malkar, N.B.2    Richet, G.3    Drauz, K.4    Fields, G.B.5
  • 82
    • 0024373738 scopus 로고
    • Structure, composition, and assembly of basement membrane
    • Leblond C.P., and Inoue S. Structure, composition, and assembly of basement membrane. Am. J. Anat. 185 (1989) 367-390
    • (1989) Am. J. Anat. , vol.185 , pp. 367-390
    • Leblond, C.P.1    Inoue, S.2
  • 83
    • 0042134847 scopus 로고    scopus 로고
    • Macrophage inhibitory cytokine-1 induces the invasiveness of gastric cancer cells by up-regulating the urokinase-type plasminogen activator system
    • Lee D.H., Yang Y., Lee S.J., Kim K.Y., Koo T.H., Shin S.M., Song K.S., Lee Y.H., Kim Y.J., Lee J.J., Choi I., and Lee J.H. Macrophage inhibitory cytokine-1 induces the invasiveness of gastric cancer cells by up-regulating the urokinase-type plasminogen activator system. Cancer Res. 63 (2003) 4648-4655
    • (2003) Cancer Res. , vol.63 , pp. 4648-4655
    • Lee, D.H.1    Yang, Y.2    Lee, S.J.3    Kim, K.Y.4    Koo, T.H.5    Shin, S.M.6    Song, K.S.7    Lee, Y.H.8    Kim, Y.J.9    Lee, J.J.10    Choi, I.11    Lee, J.H.12
  • 85
    • 0028151407 scopus 로고
    • Complete primary structure of the human type IV collagen alpha 4(IV) chain. Comparison with structure and expression of the other alpha (IV) chains
    • Leinonen A., Mariyama M., Mochizuki T., Tryggvason K., and Reeders S.T. Complete primary structure of the human type IV collagen alpha 4(IV) chain. Comparison with structure and expression of the other alpha (IV) chains. J. Biol. Chem. 269 (1994) 26172-26177
    • (1994) J. Biol. Chem. , vol.269 , pp. 26172-26177
    • Leinonen, A.1    Mariyama, M.2    Mochizuki, T.3    Tryggvason, K.4    Reeders, S.T.5
  • 86
    • 0034698054 scopus 로고    scopus 로고
    • Basement membrane zone type XV collagen is a disulfide-bonded chondroitin sulfate proteoglycan in human tissues and cultured cells
    • Li D., Clark C.C., and Myers J.C. Basement membrane zone type XV collagen is a disulfide-bonded chondroitin sulfate proteoglycan in human tissues and cultured cells. J. Biol. Chem. 275 (2000) 22339-22347
    • (2000) J. Biol. Chem. , vol.275 , pp. 22339-22347
    • Li, D.1    Clark, C.C.2    Myers, J.C.3
  • 88
    • 0032587548 scopus 로고    scopus 로고
    • alpha1 and alpha2 integrins mediate invasive activity of mouse mammary carcinoma cells through regulation of stromelysin-1 expression
    • Lochter A., Navre M., Werb Z., and Bissell M.J. alpha1 and alpha2 integrins mediate invasive activity of mouse mammary carcinoma cells through regulation of stromelysin-1 expression. Mol. Biol. Cell 10 (1999) 271-282
    • (1999) Mol. Biol. Cell , vol.10 , pp. 271-282
    • Lochter, A.1    Navre, M.2    Werb, Z.3    Bissell, M.J.4
  • 91
    • 0021700693 scopus 로고
    • The ultrastructural organization and architecture of basement membranes
    • Madri J.A., Pratt B.M., Yurchenco P.D., and Furthmayr H. The ultrastructural organization and architecture of basement membranes. Ciba. Found. Symp. 108 (1984) 6-24
    • (1984) Ciba. Found. Symp. , vol.108 , pp. 6-24
    • Madri, J.A.1    Pratt, B.M.2    Yurchenco, P.D.3    Furthmayr, H.4
  • 92
    • 0034604650 scopus 로고    scopus 로고
    • Two RGD-independent alpha vbeta 3 integrin binding sites on tumstatin regulate distinct anti-tumor properties
    • Maeshima Y., Colorado P.C., and Kalluri R. Two RGD-independent alpha vbeta 3 integrin binding sites on tumstatin regulate distinct anti-tumor properties. J. Biol. Chem. 275 (2000) 23745-23750
    • (2000) J. Biol. Chem. , vol.275 , pp. 23745-23750
    • Maeshima, Y.1    Colorado, P.C.2    Kalluri, R.3
  • 98
    • 0035851913 scopus 로고    scopus 로고
    • EGF-R signaling through Fyn kinase disrupts the function of integrin alpha6beta4 at hemidesmosomes: Role in epithelial cell migration and carcinoma invasion
    • Mariotti A., Kedeshian P.A., Dans M., Curatola A.M., Gagnoux-Palacios L., and Giancotti F.G. EGF-R signaling through Fyn kinase disrupts the function of integrin alpha6beta4 at hemidesmosomes: Role in epithelial cell migration and carcinoma invasion. J. Cell. Biol. 155 (2001) 447-458
    • (2001) J. Cell. Biol. , vol.155 , pp. 447-458
    • Mariotti, A.1    Kedeshian, P.A.2    Dans, M.3    Curatola, A.M.4    Gagnoux-Palacios, L.5    Giancotti, F.G.6
  • 99
    • 0028106032 scopus 로고
    • Complete primary structure of the human alpha 3(IV) collagen chain. Coexpression of the alpha 3(IV) and alpha 4(IV) collagen chains in human tissues
    • Mariyama M., Leinonen A., Mochizuki T., Tryggvason K., and Reeders S.T. Complete primary structure of the human alpha 3(IV) collagen chain. Coexpression of the alpha 3(IV) and alpha 4(IV) collagen chains in human tissues. J. Biol. Chem. 269 (1994) 23013-23017
    • (1994) J. Biol. Chem. , vol.269 , pp. 23013-23017
    • Mariyama, M.1    Leinonen, A.2    Mochizuki, T.3    Tryggvason, K.4    Reeders, S.T.5
  • 100
    • 0034848340 scopus 로고    scopus 로고
    • The role of collagen-derived proteolytic fragments in angiogenesis
    • Marneros A.G., and Olsen B.R. The role of collagen-derived proteolytic fragments in angiogenesis. Matrix Biol. 20 (2001) 337-345
    • (2001) Matrix Biol. , vol.20 , pp. 337-345
    • Marneros, A.G.1    Olsen, B.R.2
  • 103
    • 0042344925 scopus 로고    scopus 로고
    • Angiogenesis. A boost for tumor starvation
    • Marx J. Angiogenesis. A boost for tumor starvation. Science 301 (2003) 452-454
    • (2003) Science , vol.301 , pp. 452-454
    • Marx, J.1
  • 104
    • 0002606253 scopus 로고    scopus 로고
    • The urokinase plasminogen activator system in cancer: Implications for tumor angiogenesis and metastasis
    • Mazar A.P., Henkin J., and Goldfarb R.H. The urokinase plasminogen activator system in cancer: Implications for tumor angiogenesis and metastasis. Angiogenesis 3 (1999) 15-32
    • (1999) Angiogenesis , vol.3 , pp. 15-32
    • Mazar, A.P.1    Henkin, J.2    Goldfarb, R.H.3
  • 106
    • 0028863141 scopus 로고
    • A peptide model of basement membrane collagen alpha 1 (IV) 531-543 binds the alpha 3 beta 1 integrin
    • Miles A.J., Knutson J.R., Skubitz A.P., Furcht L.T., McCarthy J.B., and Fields G.B. A peptide model of basement membrane collagen alpha 1 (IV) 531-543 binds the alpha 3 beta 1 integrin. J. Biol. Chem. 270 (1995) 29047-29050
    • (1995) J. Biol. Chem. , vol.270 , pp. 29047-29050
    • Miles, A.J.1    Knutson, J.R.2    Skubitz, A.P.3    Furcht, L.T.4    McCarthy, J.B.5    Fields, G.B.6
  • 107
    • 0028169716 scopus 로고
    • The human alpha 1(XV) collagen chain contains a large amino-terminal non-triple helical domain with a tandem repeat structure and homology to alpha 1(XVIII) collagen
    • Muragaki Y., Abe N., Ninomiya Y., Olsen B.R., and Ooshima A. The human alpha 1(XV) collagen chain contains a large amino-terminal non-triple helical domain with a tandem repeat structure and homology to alpha 1(XVIII) collagen. J. Biol. Chem. 269 (1994) 4042-4046
    • (1994) J. Biol. Chem. , vol.269 , pp. 4042-4046
    • Muragaki, Y.1    Abe, N.2    Ninomiya, Y.3    Olsen, B.R.4    Ooshima, A.5
  • 108
    • 0028981205 scopus 로고
    • Mouse Col18a1 is expressed in a tissue-specific manner as three alternative variants and is localized in basement membrane zones
    • Muragaki Y., Timmons S., Griffith C.M., Oh S.P., Fadel B., Quertermous T., and Olsen B.R. Mouse Col18a1 is expressed in a tissue-specific manner as three alternative variants and is localized in basement membrane zones. Proc. Natl. Acad. Sci. USA 92 (1995) 8763-8767
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8763-8767
    • Muragaki, Y.1    Timmons, S.2    Griffith, C.M.3    Oh, S.P.4    Fadel, B.5    Quertermous, T.6    Olsen, B.R.7
  • 109
    • 0345335480 scopus 로고    scopus 로고
    • Collagen XVIII is localized in sinusoids and basement membrane zones and expressed by hepatocytes and activated stellate cells in fibrotic human liver
    • Musso O., Rehn M., Saarela J., Theret N., Lietard J., Hintikka, Lotrian D., Campion J.P., Pihlajaniemi T., and Clement B. Collagen XVIII is localized in sinusoids and basement membrane zones and expressed by hepatocytes and activated stellate cells in fibrotic human liver. Hepatology 28 (1998) 98-107
    • (1998) Hepatology , vol.28 , pp. 98-107
    • Musso, O.1    Rehn, M.2    Saarela, J.3    Theret, N.4    Lietard, J.5    Hintikka6    Lotrian, D.7    Campion, J.P.8    Pihlajaniemi, T.9    Clement, B.10
  • 110
    • 0035132924 scopus 로고    scopus 로고
    • Tumor progression is associated with a significant decrease in the expression of the endostatin precursor collagen XVIII in human hepatocellular carcinomas
    • Musso O., Rehn M., Theret N., Turlin B., Bioulac-Sage P., Lotrian D., Campion J.P., Pihlajaniemi T., and Clement B. Tumor progression is associated with a significant decrease in the expression of the endostatin precursor collagen XVIII in human hepatocellular carcinomas. Cancer Res. 61 (2001) 45-49
    • (2001) Cancer Res. , vol.61 , pp. 45-49
    • Musso, O.1    Rehn, M.2    Theret, N.3    Turlin, B.4    Bioulac-Sage, P.5    Lotrian, D.6    Campion, J.P.7    Pihlajaniemi, T.8    Clement, B.9
  • 111
    • 0029952102 scopus 로고    scopus 로고
    • Type XV collagen exhibits a widespread distribution in human tissues but a distinct localization in basement membrane zones
    • Myers J.C., Dion A.S., Abraham V., and Amenta P.S. Type XV collagen exhibits a widespread distribution in human tissues but a distinct localization in basement membrane zones. Cell Tissue Res. 286 (1996) 493-505
    • (1996) Cell Tissue Res. , vol.286 , pp. 493-505
    • Myers, J.C.1    Dion, A.S.2    Abraham, V.3    Amenta, P.S.4
  • 112
    • 0025360098 scopus 로고
    • Molecular cloning of alpha 5(IV) collagen and assignment of the gene to the region of the X chromosome containing the Alport syndrome locus
    • Myers J.C., Jones T.A., Pohjolainen E.R., Kadri A.S., Goddard A.D., Sheer D., Solomon E., and Pihlajaniemi T. Molecular cloning of alpha 5(IV) collagen and assignment of the gene to the region of the X chromosome containing the Alport syndrome locus. Am. J. Hum. Genet. 46 (1990) 1024-1033
    • (1990) Am. J. Hum. Genet. , vol.46 , pp. 1024-1033
    • Myers, J.C.1    Jones, T.A.2    Pohjolainen, E.R.3    Kadri, A.S.4    Goddard, A.D.5    Sheer, D.6    Solomon, E.7    Pihlajaniemi, T.8
  • 113
    • 0029965589 scopus 로고    scopus 로고
    • A mechanism for regulation of melanoma invasion. Ligation of alpha6beta1 integrin by laminin G peptides
    • Nakahara H., Nomizu M., Akiyama S.K., Yamada Y., Yeh Y., and Chen W.T. A mechanism for regulation of melanoma invasion. Ligation of alpha6beta1 integrin by laminin G peptides. J. Biol. Chem. 271 (1996) 27221-27224
    • (1996) J. Biol. Chem. , vol.271 , pp. 27221-27224
    • Nakahara, H.1    Nomizu, M.2    Akiyama, S.K.3    Yamada, Y.4    Yeh, Y.5    Chen, W.T.6
  • 114
    • 0142219888 scopus 로고    scopus 로고
    • Direct activation of pro-matrix metalloproteinase-2 by leukolysin/membrane-type 6 matrix metalloproteinase/matrix metalloproteinase 25 at the asn(109)-Tyr bond
    • Nie J., and Pei D. Direct activation of pro-matrix metalloproteinase-2 by leukolysin/membrane-type 6 matrix metalloproteinase/matrix metalloproteinase 25 at the asn(109)-Tyr bond. Cancer Res. 63 (2003) 6758-6762
    • (2003) Cancer Res. , vol.63 , pp. 6758-6762
    • Nie, J.1    Pei, D.2
  • 116
    • 0026451947 scopus 로고
    • Human melanoma cells derived from lymphatic metastases use integrin alpha v beta 3 to adhere to lymph node vitronectin
    • Nip J., Shibata H., Loskutoff D.J., Cheresh D.A., and Brodt P. Human melanoma cells derived from lymphatic metastases use integrin alpha v beta 3 to adhere to lymph node vitronectin. J. Clin. Invest. 90 (1992) 1413
    • (1992) J. Clin. Invest. , vol.90 , pp. 1413
    • Nip, J.1    Shibata, H.2    Loskutoff, D.J.3    Cheresh, D.A.4    Brodt, P.5
  • 117
    • 0001033082 scopus 로고
    • Isolation and sequencing of cDNAs for proteins with multiple domains of Gly-Xaa-Yaa repeats identify a distinct family of collagenous proteins
    • Oh S.P., Kamagata Y., Muragaki Y., Timmons S., Ooshima A., and Olsen B.R. Isolation and sequencing of cDNAs for proteins with multiple domains of Gly-Xaa-Yaa repeats identify a distinct family of collagenous proteins. Proc. Natl. Acad. Sci. USA 91 (1994) 4229-4233
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4229-4233
    • Oh, S.P.1    Kamagata, Y.2    Muragaki, Y.3    Timmons, S.4    Ooshima, A.5    Olsen, B.R.6
  • 118
    • 0028210848 scopus 로고
    • Cloning of cDNA and genomic DNA encoding human type XVIII collagen and localization of the alpha 1(XVIII) collagen gene to mouse chromosome 10 and human chromosome 21
    • Oh S.P., Warman M.L., Seldin M.F., Cheng S.D., Knoll J.H., Timmons S., and Olsen B.R. Cloning of cDNA and genomic DNA encoding human type XVIII collagen and localization of the alpha 1(XVIII) collagen gene to mouse chromosome 10 and human chromosome 21. Genomics 19 (1994) 494-499
    • (1994) Genomics , vol.19 , pp. 494-499
    • Oh, S.P.1    Warman, M.L.2    Seldin, M.F.3    Cheng, S.D.4    Knoll, J.H.5    Timmons, S.6    Olsen, B.R.7
  • 119
    • 0034878621 scopus 로고    scopus 로고
    • Coordinate expression of membrane type-matrix metalloproteinases-2 and 3 (MT2-MMP and MT3-MMP) and matrix metalloproteinase-2 (MMP-2) in primary and metastatic melanoma cells
    • Ohnishi Y., Tajima S., and Ishibashi A. Coordinate expression of membrane type-matrix metalloproteinases-2 and 3 (MT2-MMP and MT3-MMP) and matrix metalloproteinase-2 (MMP-2) in primary and metastatic melanoma cells. Eur. J. Dermatol. 11 (2001) 420-423
    • (2001) Eur. J. Dermatol. , vol.11 , pp. 420-423
    • Ohnishi, Y.1    Tajima, S.2    Ishibashi, A.3
  • 120
    • 3242805932 scopus 로고    scopus 로고
    • The role of cell adhesion molecule in cancer progression and its application in cancer therapy
    • Okegawa T., Pong R.C., Li Y., and Hsieh J.T. The role of cell adhesion molecule in cancer progression and its application in cancer therapy. Acta Biochim. Pol. 51 (2004) 445-457
    • (2004) Acta Biochim. Pol. , vol.51 , pp. 445-457
    • Okegawa, T.1    Pong, R.C.2    Li, Y.3    Hsieh, J.T.4
  • 121
    • 0033137299 scopus 로고    scopus 로고
    • Clinocopathologic significance of laminin-5 gamma2 chain expression in squamous cell carcinoma of the tongue: immunohistochemical analysis of 67 lesions
    • Ono Y., Nakanishi Y., Ino Y., Niki T., Yamada T., Yoshimura K., Saikawa M., Nakajima T., and Hirohashi S. Clinocopathologic significance of laminin-5 gamma2 chain expression in squamous cell carcinoma of the tongue: immunohistochemical analysis of 67 lesions. Cancer 85 (1999) 2315-2321
    • (1999) Cancer , vol.85 , pp. 2315-2321
    • Ono, Y.1    Nakanishi, Y.2    Ino, Y.3    Niki, T.4    Yamada, T.5    Yoshimura, K.6    Saikawa, M.7    Nakajima, T.8    Hirohashi, S.9
  • 123
    • 0032832479 scopus 로고    scopus 로고
    • Regulation of angiostatin production by matrix metalloproteinase-2 in a model of concomitant resistance [In Process Citation]
    • O'Reilly M.S., Wiederschain D., Stetler-Stevenson W.G., Folkman J., and Moses M.A. Regulation of angiostatin production by matrix metalloproteinase-2 in a model of concomitant resistance [In Process Citation]. J. Biol. Chem. 274 (1999) 29568-29571
    • (1999) J. Biol. Chem. , vol.274 , pp. 29568-29571
    • O'Reilly, M.S.1    Wiederschain, D.2    Stetler-Stevenson, W.G.3    Folkman, J.4    Moses, M.A.5
  • 124
    • 0141621149 scopus 로고    scopus 로고
    • Canstatin inhibits Akt activation and induces Fas-dependent apoptosis in endothelial cells
    • Panka D.J., and Mier J.W. Canstatin inhibits Akt activation and induces Fas-dependent apoptosis in endothelial cells. J. Biol. Chem. 278 (2003) 37632-37636
    • (2003) J. Biol. Chem. , vol.278 , pp. 37632-37636
    • Panka, D.J.1    Mier, J.W.2
  • 125
    • 0034650403 scopus 로고    scopus 로고
    • A specific sequence of the noncollagenous domain of the alpha3(IV) chain of type IV collagen inhibits expression and activation of matrix metalloproteinases by tumor cells
    • Pasco S., Han J., Gillery P., Bellon G., Maquart F.X., Borel J.P., Kefalides N.A., and Monboisse J.C. A specific sequence of the noncollagenous domain of the alpha3(IV) chain of type IV collagen inhibits expression and activation of matrix metalloproteinases by tumor cells. Cancer Res. 60 (2000) 467-473
    • (2000) Cancer Res. , vol.60 , pp. 467-473
    • Pasco, S.1    Han, J.2    Gillery, P.3    Bellon, G.4    Maquart, F.X.5    Borel, J.P.6    Kefalides, N.A.7    Monboisse, J.C.8
  • 126
    • 0034693240 scopus 로고    scopus 로고
    • The alpha 3(IV)185-206 peptide from noncollagenous domain 1 of type IV collagen interacts with a novel binding site on the beta 3 subunit of integrin alpha Vbeta 3 and stimulates focal adhesion kinase and phosphatidylinositol 3-kinase phosphorylation
    • Pasco S., Monboisse J.C., and Kieffer N. The alpha 3(IV)185-206 peptide from noncollagenous domain 1 of type IV collagen interacts with a novel binding site on the beta 3 subunit of integrin alpha Vbeta 3 and stimulates focal adhesion kinase and phosphatidylinositol 3-kinase phosphorylation. J. Biol. Chem. 275 (2000) 32999-33007
    • (2000) J. Biol. Chem. , vol.275 , pp. 32999-33007
    • Pasco, S.1    Monboisse, J.C.2    Kieffer, N.3
  • 127
    • 1342300683 scopus 로고    scopus 로고
    • Control of melanoma progression by various matrikines from basement membrane macromolecules
    • Pasco S., Ramont L., Maquart F.X., and Monboisse J.C. Control of melanoma progression by various matrikines from basement membrane macromolecules. Crit. Rev. Oncol. Hematol. 49 (2004) 221-233
    • (2004) Crit. Rev. Oncol. Hematol. , vol.49 , pp. 221-233
    • Pasco, S.1    Ramont, L.2    Maquart, F.X.3    Monboisse, J.C.4
  • 128
    • 15444352707 scopus 로고    scopus 로고
    • Angiostatin-converting enzyme activities of human matrilysin (MMP-7) and gelatinase B/type IV collagenase (MMP-9)
    • Patterson B.C., and Sang Q.A. Angiostatin-converting enzyme activities of human matrilysin (MMP-7) and gelatinase B/type IV collagenase (MMP-9). J. Biol. Chem. 272 (1997) 28823-28825
    • (1997) J. Biol. Chem. , vol.272 , pp. 28823-28825
    • Patterson, B.C.1    Sang, Q.A.2
  • 129
    • 0034677760 scopus 로고    scopus 로고
    • New functions for non-collagenous domains of human collagen type IV. Novel integrin ligands inhibiting angiogenesis and tumor growth in vivo
    • Petitclerc E., Boutaud A., Prestayko A., Xu J., Sado Y., Ninomiya Y., Sarras Jr. M.P., Hudson B.G., and Brooks P.C. New functions for non-collagenous domains of human collagen type IV. Novel integrin ligands inhibiting angiogenesis and tumor growth in vivo. J. Biol. Chem. 275 (2000) 8051-8061
    • (2000) J. Biol. Chem. , vol.275 , pp. 8051-8061
    • Petitclerc, E.1    Boutaud, A.2    Prestayko, A.3    Xu, J.4    Sado, Y.5    Ninomiya, Y.6    Sarras Jr., M.P.7    Hudson, B.G.8    Brooks, P.C.9
  • 131
    • 0034007381 scopus 로고    scopus 로고
    • Elevated matrix metalloprotease and angiostatin levels in integrin alpha 1 knockout mice cause reduced tumor vascularization
    • Pozzi A., Moberg P.E., Miles L.A., Wagner S., Soloway P., and Gardner H.A. Elevated matrix metalloprotease and angiostatin levels in integrin alpha 1 knockout mice cause reduced tumor vascularization. Proc. Natl. Acad. Sci. USA 97 (2000) 2202-2207
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2202-2207
    • Pozzi, A.1    Moberg, P.E.2    Miles, L.A.3    Wagner, S.4    Soloway, P.5    Gardner, H.A.6
  • 132
    • 0037050259 scopus 로고    scopus 로고
    • Low plasma levels of matrix metalloproteinase 9 permit increased tumor angiogenesis
    • Pozzi A., Le Vine W.F., and Gardner H.A. Low plasma levels of matrix metalloproteinase 9 permit increased tumor angiogenesis. Oncogene 21 (2002) 272-281
    • (2002) Oncogene , vol.21 , pp. 272-281
    • Pozzi, A.1    Le Vine, W.F.2    Gardner, H.A.3
  • 133
    • 0348198389 scopus 로고    scopus 로고
    • Integrins: Sensors of extracellular matrix and modulators of cell function
    • Pozzi A., and Zent R. Integrins: Sensors of extracellular matrix and modulators of cell function. Nephron. Exp. Nephrol. 94 (2003) e77-e84
    • (2003) Nephron. Exp. Nephrol. , vol.94
    • Pozzi, A.1    Zent, R.2
  • 134
    • 0028173385 scopus 로고
    • The gamma 2 chain of kalinin/laminin 5 is preferentially expressed in invading malignant cells in human cancers
    • Pyke C., Romer J., Kallunki P., Lund L.R., Ralfkiaer E., Dano K., and Tryggvason K. The gamma 2 chain of kalinin/laminin 5 is preferentially expressed in invading malignant cells in human cancers. Am. J. Pathol. 145 (1994) 782-791
    • (1994) Am. J. Pathol. , vol.145 , pp. 782-791
    • Pyke, C.1    Romer, J.2    Kallunki, P.3    Lund, L.R.4    Ralfkiaer, E.5    Dano, K.6    Tryggvason, K.7
  • 135
    • 0029144854 scopus 로고
    • Laminin-5 is a marker of invading cancer cells in some human carcinomas and is coexpressed with the receptor for urokinase plasminogen activator in budding cancer cells in colon adenocarcinomas
    • Pyke C., Salo S., Ralfkiaer E., Romer J., Dano K., and Tryggvason K. Laminin-5 is a marker of invading cancer cells in some human carcinomas and is coexpressed with the receptor for urokinase plasminogen activator in budding cancer cells in colon adenocarcinomas. Cancer Res. 55 (1995) 4132-4139
    • (1995) Cancer Res. , vol.55 , pp. 4132-4139
    • Pyke, C.1    Salo, S.2    Ralfkiaer, E.3    Romer, J.4    Dano, K.5    Tryggvason, K.6
  • 136
    • 0036995876 scopus 로고    scopus 로고
    • Motility cues in the tumor microenvironment
    • Quaranta V. Motility cues in the tumor microenvironment. Differentiation 70 (2002) 590-598
    • (2002) Differentiation , vol.70 , pp. 590-598
    • Quaranta, V.1
  • 137
    • 0141958793 scopus 로고    scopus 로고
    • Differential expression of alpha1 (IV) and alpha5 (IV) collagen chains in basal-cell carcinoma
    • Quatresooz P., Martalo O., and Pierard G.E. Differential expression of alpha1 (IV) and alpha5 (IV) collagen chains in basal-cell carcinoma. J. Cutan. Pathol. 30 (2003) 548-552
    • (2003) J. Cutan. Pathol. , vol.30 , pp. 548-552
    • Quatresooz, P.1    Martalo, O.2    Pierard, G.E.3
  • 139
    • 0028174283 scopus 로고
    • Primary structure of the alpha 1 chain of mouse type XVIII collagen, partial structure of the corresponding gene, and comparison of the alpha 1(XVIII) chain with its homologue, the alpha 1(XV) collagen chain
    • Rehn M., Hintikka E., and Pihlajaniemi T. Primary structure of the alpha 1 chain of mouse type XVIII collagen, partial structure of the corresponding gene, and comparison of the alpha 1(XVIII) chain with its homologue, the alpha 1(XV) collagen chain. J. Biol. Chem. 269 (1994) 13929-13935
    • (1994) J. Biol. Chem. , vol.269 , pp. 13929-13935
    • Rehn, M.1    Hintikka, E.2    Pihlajaniemi, T.3
  • 140
    • 0028176183 scopus 로고
    • Alpha 1(XVIII), a collagen chain with frequent interruptions in the collagenous sequence, a distinct tissue distribution, and homology with type XV collagen
    • Rehn M., and Pihlajaniemi T. Alpha 1(XVIII), a collagen chain with frequent interruptions in the collagenous sequence, a distinct tissue distribution, and homology with type XV collagen. Proc. Natl. Acad. Sci. USA 91 (1994) 4234-4238
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4234-4238
    • Rehn, M.1    Pihlajaniemi, T.2
  • 142
    • 0031830711 scopus 로고    scopus 로고
    • The short and long forms of type XVIII collagen show clear tissue specificities in their expression and location in basement membrane zones in humans
    • Saarela J., Rehn M., Oikarinen A., Autio-Harmainen H., and Pihlajaniemi T. The short and long forms of type XVIII collagen show clear tissue specificities in their expression and location in basement membrane zones in humans. Am. J. Pathol. 153 (1998) 611-626
    • (1998) Am. J. Pathol. , vol.153 , pp. 611-626
    • Saarela, J.1    Rehn, M.2    Oikarinen, A.3    Autio-Harmainen, H.4    Pihlajaniemi, T.5
  • 143
    • 0032160033 scopus 로고    scopus 로고
    • Complex role of matrix metalloproteinases in angiogenesis
    • Sang Q.X. Complex role of matrix metalloproteinases in angiogenesis. Cell Res. 8 (1998) 171-177
    • (1998) Cell Res. , vol.8 , pp. 171-177
    • Sang, Q.X.1
  • 144
    • 0034283571 scopus 로고    scopus 로고
    • Endostatins derived from collagens XV and XVIII differ in structural and binding properties, tissue distribution and anti-angiogenic activity
    • Sasaki T., Larsson H., Tisi D., Claesson-Welsh L., Hohenester E., and Timpl R. Endostatins derived from collagens XV and XVIII differ in structural and binding properties, tissue distribution and anti-angiogenic activity. J. Mol. Biol. 301 (2000) 1179-1190
    • (2000) J. Mol. Biol. , vol.301 , pp. 1179-1190
    • Sasaki, T.1    Larsson, H.2    Tisi, D.3    Claesson-Welsh, L.4    Hohenester, E.5    Timpl, R.6
  • 146
    • 0030019731 scopus 로고    scopus 로고
    • Membrane-type matrix metalloproteinases (MT-MMPs) in tumor metastasis
    • Sato H., and Seiki M. Membrane-type matrix metalloproteinases (MT-MMPs) in tumor metastasis. J. Biochem. (Tokyo) 119 (1996) 209-215
    • (1996) J. Biochem. (Tokyo) , vol.119 , pp. 209-215
    • Sato, H.1    Seiki, M.2
  • 147
    • 0037437146 scopus 로고    scopus 로고
    • Binding to EGF receptor of a laminin-5 EGF-like fragment liberated during MMP-dependent mammary gland involution
    • Schenk S., Hintermann E., Bilban M., Koshikawa N., Hojilla C., Khokha R., and Quaranta V. Binding to EGF receptor of a laminin-5 EGF-like fragment liberated during MMP-dependent mammary gland involution. J. Cell. Biol. 161 (2003) 197-209
    • (2003) J. Cell. Biol. , vol.161 , pp. 197-209
    • Schenk, S.1    Hintermann, E.2    Bilban, M.3    Koshikawa, N.4    Hojilla, C.5    Khokha, R.6    Quaranta, V.7
  • 149
    • 0031459892 scopus 로고    scopus 로고
    • Angiogenesis promoted by vascular endothelial growth factor: Regulation through alpha1beta1 and alpha2beta1 integrins
    • Senger D.R., Claffey K.P., Benes J.E., Perruzzi C.A., Sergiou A.P., and Detmar M. Angiogenesis promoted by vascular endothelial growth factor: Regulation through alpha1beta1 and alpha2beta1 integrins. Proc. Natl. Acad. Sci. USA 94 (1997) 13612-13617
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13612-13617
    • Senger, D.R.1    Claffey, K.P.2    Benes, J.E.3    Perruzzi, C.A.4    Sergiou, A.P.5    Detmar, M.6
  • 151
    • 0038364216 scopus 로고    scopus 로고
    • The urokinase plasminogen activator system in cancer: Recent advances and implication for prognosis and therapy
    • Sidenius N., and Blasi F. The urokinase plasminogen activator system in cancer: Recent advances and implication for prognosis and therapy. Cancer Metastasis Rev. 22 (2003) 205-222
    • (2003) Cancer Metastasis Rev. , vol.22 , pp. 205-222
    • Sidenius, N.1    Blasi, F.2
  • 153
    • 0029915884 scopus 로고    scopus 로고
    • Expression of alpha 6 and beta 4 integrins in serous ovarian carcinoma correlates with expression of the basement membrane protein laminin
    • Skubitz A.P., Bast Jr. R.C., Wayner E.A., Letourneau P.C., and Wilke M.S. Expression of alpha 6 and beta 4 integrins in serous ovarian carcinoma correlates with expression of the basement membrane protein laminin. Am. J. Pathol. 148 (1996) 1445-1461
    • (1996) Am. J. Pathol. , vol.148 , pp. 1445-1461
    • Skubitz, A.P.1    Bast Jr., R.C.2    Wayner, E.A.3    Letourneau, P.C.4    Wilke, M.S.5
  • 155
    • 0021728249 scopus 로고
    • Cysteine proteinases and metastasis
    • Sloane B.F., and Honn K.V. Cysteine proteinases and metastasis. Cancer Metastasis Rev. 3 (1984) 249-263
    • (1984) Cancer Metastasis Rev. , vol.3 , pp. 249-263
    • Sloane, B.F.1    Honn, K.V.2
  • 157
    • 0023631976 scopus 로고
    • Complete primary structure of the alpha 1-chain of human basement membrane (type IV) collagen
    • Soininen R., Haka-Risku T., Prockop D.J., and Tryggvason K. Complete primary structure of the alpha 1-chain of human basement membrane (type IV) collagen. FEBS Lett. 225 (1987) 188-194
    • (1987) FEBS Lett. , vol.225 , pp. 188-194
    • Soininen, R.1    Haka-Risku, T.2    Prockop, D.J.3    Tryggvason, K.4
  • 158
    • 0038575443 scopus 로고    scopus 로고
    • Extracellular matrix remodelling: The role of matrix metalloproteinases
    • Stamenkovic I. Extracellular matrix remodelling: The role of matrix metalloproteinases. J. Pathol. 200 (2003) 448-464
    • (2003) J. Pathol. , vol.200 , pp. 448-464
    • Stamenkovic, I.1
  • 159
    • 0035000670 scopus 로고    scopus 로고
    • Proteases in invasion: Matrix metalloproteinases
    • Stetler-Stevenson W.G., and Yu A.E. Proteases in invasion: Matrix metalloproteinases. Semin. Cancer Biol. 11 (2001) 143-152
    • (2001) Semin. Cancer Biol. , vol.11 , pp. 143-152
    • Stetler-Stevenson, W.G.1    Yu, A.E.2
  • 160
    • 0031914189 scopus 로고    scopus 로고
    • Prognostic value of alpha 6 beta 4 integrin expression in breast carcinomas is affected by laminin production from tumor cells
    • Tagliabue E., Ghirelli C., Squicciarini P., Aiello P., Colnaghi M.I., and Menard S. Prognostic value of alpha 6 beta 4 integrin expression in breast carcinomas is affected by laminin production from tumor cells. Clin. Cancer Res. 4 (1998) 407-410
    • (1998) Clin. Cancer Res. , vol.4 , pp. 407-410
    • Tagliabue, E.1    Ghirelli, C.2    Squicciarini, P.3    Aiello, P.4    Colnaghi, M.I.5    Menard, S.6
  • 161
    • 0019781637 scopus 로고
    • A network model for the organization of type IV collagen molecules in basement membranes
    • Timpl R., Wiedemann H., van Delden V., Furthmayr H., and Kuhn K. A network model for the organization of type IV collagen molecules in basement membranes. Eur. J. Biochem. 120 (1981) 203-211
    • (1981) Eur. J. Biochem. , vol.120 , pp. 203-211
    • Timpl, R.1    Wiedemann, H.2    van Delden, V.3    Furthmayr, H.4    Kuhn, K.5
  • 162
    • 0038713422 scopus 로고    scopus 로고
    • Membrane type-1-matrix metalloproteinase expressed by prostate carcinoma cells cleaves human laminin-5 beta3 chain and induces cell migration
    • Udayakumar T.S., Chen M.L., Bair E.L., Von Bredow D.C., Cress A.E., Nagle R.B., and owden G.T. Membrane type-1-matrix metalloproteinase expressed by prostate carcinoma cells cleaves human laminin-5 beta3 chain and induces cell migration. Cancer Res. 63 (2003) 2292-2299
    • (2003) Cancer Res. , vol.63 , pp. 2292-2299
    • Udayakumar, T.S.1    Chen, M.L.2    Bair, E.L.3    Von Bredow, D.C.4    Cress, A.E.5    Nagle, R.B.6    owden, G.T.7
  • 163
    • 0031595984 scopus 로고    scopus 로고
    • Separate functions of alpha2beta1 and alpha3beta1 integrins in the metastatic process of human gastric carcinoma
    • Ura H., Denno R., Hirata K., Yamaguchi K., and Yasoshima T. Separate functions of alpha2beta1 and alpha3beta1 integrins in the metastatic process of human gastric carcinoma. Surg. Today 28 (1998) 1001-1006
    • (1998) Surg. Today , vol.28 , pp. 1001-1006
    • Ura, H.1    Denno, R.2    Hirata, K.3    Yamaguchi, K.4    Yasoshima, T.5
  • 164
    • 0025881189 scopus 로고
    • Characterization of a type IV collagen major cell binding site with affinity to the alpha 1 beta 1 and the alpha 2 beta 1 integrins
    • Vandenberg P., Kern A., Ries A., Luckenbill-Edds L., Mann K., and Kuhn K. Characterization of a type IV collagen major cell binding site with affinity to the alpha 1 beta 1 and the alpha 2 beta 1 integrins. J. Cell. Biol. 113 (1991) 1475-1483
    • (1991) J. Cell. Biol. , vol.113 , pp. 1475-1483
    • Vandenberg, P.1    Kern, A.2    Ries, A.3    Luckenbill-Edds, L.4    Mann, K.5    Kuhn, K.6
  • 165
    • 2442555007 scopus 로고    scopus 로고
    • An endostatin-derived peptide interacts with integrins and regulates actin cytoskeleton and migration of endothelial cells
    • Wickstrom S.A., Alitalo K., and Keski-Oja J. An endostatin-derived peptide interacts with integrins and regulates actin cytoskeleton and migration of endothelial cells. J. Biol. Chem. 279 (2004) 20178-20185
    • (2004) J. Biol. Chem. , vol.279 , pp. 20178-20185
    • Wickstrom, S.A.1    Alitalo, K.2    Keski-Oja, J.3
  • 167
    • 0034906939 scopus 로고    scopus 로고
    • Expression of the gamma(2) chain of laminin-5 at the invasive front is associated with recurrence and poor prognosis in human esophageal squamous cell carcinoma
    • Yamamoto H., Itoh F., Iku S., Hosokawa M., and Imai K. Expression of the gamma(2) chain of laminin-5 at the invasive front is associated with recurrence and poor prognosis in human esophageal squamous cell carcinoma. Clin. Cancer Res. 7 (2001) 896-900
    • (2001) Clin. Cancer Res. , vol.7 , pp. 896-900
    • Yamamoto, H.1    Itoh, F.2    Iku, S.3    Hosokawa, M.4    Imai, K.5
  • 168
    • 0031884265 scopus 로고    scopus 로고
    • Cathepsin B and human tumor progression
    • Yan S., Sameni M., and Sloane B.F. Cathepsin B and human tumor progression. Biol. Chem. 379 (1998) 113-123
    • (1998) Biol. Chem. , vol.379 , pp. 113-123
    • Yan, S.1    Sameni, M.2    Sloane, B.F.3
  • 169
    • 0346365371 scopus 로고    scopus 로고
    • Integrin alpha1beta1 and alpha2beta1 are the key regulators of hepatocarcinoma cell invasion across the fibrotic matrix microenvironment
    • Yang C., Zeisberg M., Lively J.C., Nyberg P., Afdhal N., and Kalluri R. Integrin alpha1beta1 and alpha2beta1 are the key regulators of hepatocarcinoma cell invasion across the fibrotic matrix microenvironment. Cancer Res. 63 (2003) 8312-8317
    • (2003) Cancer Res. , vol.63 , pp. 8312-8317
    • Yang, C.1    Zeisberg, M.2    Lively, J.C.3    Nyberg, P.4    Afdhal, N.5    Kalluri, R.6
  • 170
    • 0033516721 scopus 로고    scopus 로고
    • A peptide of the alpha3 chain of type IV collagen protects basement membrane against damage by PMN
    • Ziaie Z., Fawzi A., Bellon G., Monboisse J.C., and Kefalides N.A. A peptide of the alpha3 chain of type IV collagen protects basement membrane against damage by PMN. Biochem. Biophys. Res. Commun. 261 (1999) 247-250
    • (1999) Biochem. Biophys. Res. Commun. , vol.261 , pp. 247-250
    • Ziaie, Z.1    Fawzi, A.2    Bellon, G.3    Monboisse, J.C.4    Kefalides, N.A.5


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